Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.2.1.B23 extracted from

  • Hu, Y.; Luan, H.; Hao, D.; Xiao, H.; Yang, S.; Yang, L.
    Purification and characterization of a novel ginsenoside-hydrolyzing beta-D-glucosidase from the China white jade snail (Achatina fulica) (2007), Enzyme Microb. Technol., 40, 1358-1366.
No PubMed abstract available
Search for more literature for 3.2.1.B23

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
 2 * 110000, SDS-PAGE Lissachatina fulica
220000
-
 native PAGE Lissachatina fulica

Organism

Organism UniProt Comment Textmining
Lissachatina fulica
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information might be a glycoprotein Lissachatina fulica

Purification (Commentary)

Purification (Comment) Organism
-
 Lissachatina fulica

Source Tissue

Source Tissue Comment Organism Textmining
viscus
-
 Lissachatina fulica
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
162.8
-
 pH 5.0, 50°C, substrate: 4-nitrophenyl-beta-D-glucopyranoside Lissachatina fulica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ginsenoside Rb1 + H2O the enzyme hydrolyzes the 20-O-beta-D-(1->6)-glucoside and both glucosidic linkages at 3-C. The enzyme prefers the 20-C, beta-(1->6)-glucosidic bond to the 3-C, beta-(1->2)-glucosidic bond. Ginsenoside Rb1 is firstly converted to ginsenoside Rd, subsequently to ginsenoside F2, and finally to ginsenoside C-K after 24 h of incubation Lissachatina fulica ginsenoside C-K + 3 D-glucose
-
 ?
ginsenoside Rb2 + 2 H2O the enzyme hydrolyzes both glucosidic linkages at 3-C. Ginsenoside Rb2 is firstly converted to ginsenoside C-O and subsequently to ginsenoside C-Y Lissachatina fulica ginsenoside C-Y + 2 D-glucose
-
 ?
ginsenoside Rb3 + H2O the enzyme hydrolyzes both glucosidic linkages at 3-C Lissachatina fulica ginsenoside Mx + 2 D-glucose
-
 ?
ginsenoside Rc + H2O the enzyme hydrolyzes both glucosidic linkages at 3-C Lissachatina fulica ginsenoside Mc + 2 D-glucose
-
 ?
additional information the enzyme does not cleave the 20-C-beta-D-(6->1)-arabinopyranoside of ginsenoside Rb2, the 20-C-beta-D-(6->1)-xyloside of ginsenoside Rb3, the 20-O-beta-D-(6->1)-arabinofuranoide of ginsenoside Rc. The enzyme also hydrolyses 4-nitrophenyl-beta-D-glycosides, cellobiose, sophorose, methyl beta-glucopyranoside, hexyl beta-D-glucopyranoside, heptyl beta-D-glucopyranoside, decyl beta-D-glucopyranoside, dodecyl beta-D-glucopyranoside Lissachatina fulica ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 110000, SDS-PAGE Lissachatina fulica

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
 assay at Lissachatina fulica

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 50 8 h, enzyme retains full activity Lissachatina fulica
60
-
 stable for 30 min, 72% loss of activity after 30 min Lissachatina fulica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5
-
-
 Lissachatina fulica

pH Range

pH Minimum pH Maximum Comment Organism
4 6.5 pH 4.0: about 40% of maximal activity, pH 6.5: about 50% of maximal activity Lissachatina fulica

pH Stability

pH Stability pH Stability Maximum Comment Organism
4 10 retains more than 82% of its original activity after 24 h at 30°C Lissachatina fulica